Nedd8 processing enzymes in Schizosaccharomyces pombe

Jean O'Donoghue; Dawadschargal Bech-Otschir; Ida Larsen; Mairi Wallace; Rasmus Hartmann-Petersen; Colin Gordon

doi:10.1186/1471-2091-14-8

Nedd8 processing enzymes in Schizosaccharomyces pombe

Jean O'Donoghue, Dawadschargal Bech-Otschir, Ida Larsen, Mairi Wallace, Rasmus Hartmann-Petersen, Colin Gordon

Biomolecular Sciences

5 Citations (Scopus)

446 Downloads (Pure)

Abstract

Background: Conjugation of the ubiquitin-like modifier Nedd8 to cullins is critical for the function of SCF-type ubiquitin ligases and thus facilitates ubiquitin conjugation and ultimately degradation of SCF substrates, including several cell cycle regulators. Like ubiquitin, Nedd8 is produced as a precursor that must first be processed before it becomes active. In Saccharomyces cerevisiae this is carried out exclusively by the enzyme Yuh1. Results: Here we show that in the fission yeast, Schizosaccharomyces pombe, the Yuh1 orthologue, Uch1, is not the sole Nedd8 processing enzyme. Instead it appears that deubiquitylating enzymes can efficiently process the Nedd8 precursor in vivo. Conclusions: Several enzymes contribute to Nedd8 precursor processing including a number of deubiquitylating enzymes.

Original language	English
Journal	B M C Biochemistry
Volume	14
Issue number	8
Pages (from-to)	1-6
Number of pages	6
ISSN	1471-2091
DOIs	https://doi.org/10.1186/1471-2091-14-8
Publication status	Published - 2013

Access to Document

10.1186/1471-2091-14-8

Nedd8 processing...Final published version, 582 KB

http://dx.doi.org/10.1186/1471-2091-14-8

Cite this

@article{d2e8695cf79142c995760850dda38911,

title = "Nedd8 processing enzymes in Schizosaccharomyces pombe",

abstract = "Background: Conjugation of the ubiquitin-like modifier Nedd8 to cullins is critical for the function of SCF-type ubiquitin ligases and thus facilitates ubiquitin conjugation and ultimately degradation of SCF substrates, including several cell cycle regulators. Like ubiquitin, Nedd8 is produced as a precursor that must first be processed before it becomes active. In Saccharomyces cerevisiae this is carried out exclusively by the enzyme Yuh1. Results: Here we show that in the fission yeast, Schizosaccharomyces pombe, the Yuh1 orthologue, Uch1, is not the sole Nedd8 processing enzyme. Instead it appears that deubiquitylating enzymes can efficiently process the Nedd8 precursor in vivo. Conclusions: Several enzymes contribute to Nedd8 precursor processing including a number of deubiquitylating enzymes.",

author = "Jean O'Donoghue and Dawadschargal Bech-Otschir and Ida Larsen and Mairi Wallace and Rasmus Hartmann-Petersen and Colin Gordon",

year = "2013",

doi = "10.1186/1471-2091-14-8",

language = "English",

volume = "14",

pages = "1--6",

journal = "B M C Biochemistry",

issn = "1471-2091",

publisher = "BioMed Central Ltd.",

number = "8",

}

TY - JOUR

T1 - Nedd8 processing enzymes in Schizosaccharomyces pombe

AU - O'Donoghue, Jean

AU - Bech-Otschir, Dawadschargal

AU - Larsen, Ida

AU - Wallace, Mairi

AU - Hartmann-Petersen, Rasmus

AU - Gordon, Colin

PY - 2013

Y1 - 2013

N2 - Background: Conjugation of the ubiquitin-like modifier Nedd8 to cullins is critical for the function of SCF-type ubiquitin ligases and thus facilitates ubiquitin conjugation and ultimately degradation of SCF substrates, including several cell cycle regulators. Like ubiquitin, Nedd8 is produced as a precursor that must first be processed before it becomes active. In Saccharomyces cerevisiae this is carried out exclusively by the enzyme Yuh1. Results: Here we show that in the fission yeast, Schizosaccharomyces pombe, the Yuh1 orthologue, Uch1, is not the sole Nedd8 processing enzyme. Instead it appears that deubiquitylating enzymes can efficiently process the Nedd8 precursor in vivo. Conclusions: Several enzymes contribute to Nedd8 precursor processing including a number of deubiquitylating enzymes.

AB - Background: Conjugation of the ubiquitin-like modifier Nedd8 to cullins is critical for the function of SCF-type ubiquitin ligases and thus facilitates ubiquitin conjugation and ultimately degradation of SCF substrates, including several cell cycle regulators. Like ubiquitin, Nedd8 is produced as a precursor that must first be processed before it becomes active. In Saccharomyces cerevisiae this is carried out exclusively by the enzyme Yuh1. Results: Here we show that in the fission yeast, Schizosaccharomyces pombe, the Yuh1 orthologue, Uch1, is not the sole Nedd8 processing enzyme. Instead it appears that deubiquitylating enzymes can efficiently process the Nedd8 precursor in vivo. Conclusions: Several enzymes contribute to Nedd8 precursor processing including a number of deubiquitylating enzymes.

U2 - 10.1186/1471-2091-14-8

DO - 10.1186/1471-2091-14-8

M3 - Journal article

C2 - 23496905

SN - 1471-2091

VL - 14

SP - 1

EP - 6

JO - B M C Biochemistry

JF - B M C Biochemistry

IS - 8

ER -

Nedd8 processing enzymes in Schizosaccharomyces pombe

Abstract

Access to Document

Fingerprint

Cite this